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- 7Prion protein
- 2Force spectroscopy
- 2Optical tweezers
- 2Protein folding
- 2Protein misfolding
- 1Aiken, J.M.
- 1Charrunchon, Sookpichaya
- 1Gilbert, P.
- 1Johnson, C.J.
- 1Lam, Tran Hu Th
- 1Leighton, Patricia LA
Protein folding involves a stochastic search through the configurational energy landscape towards the native structure. Although most proteins have evolved to fold efficiently into a unique native structure, misfolding (the formation of non-native structures) occurs frequently in vivo causing a...
Transmissible Spongiform Encephalopathies (TSEs) are a class of fatal, infectious neurodegenerative disorders affecting the central nervous system. The critical event in the pathogenesis of TSEs is the autocatalytic conformational conversion of the cellular prion protein (PrPC) into an...
Prion diseases, are associated with the misfolded form of the prion protein (PrPSc). The prion protein (PrP) has a unique means of transferring infectious diseases, based on a misfolded conformation. However, the mechanism of formation of PrPSc remains unclear owing to difficulties in defining...
Studying the effects of mouse prion protein on mice and rat colon antibacterial gene expression profilingDownload
The objectives of this thesis research are: 1) to evaluate whether there is interspecies translocation of mouse recombinant prion protein (moPrP) through colon tissue of rats; 2) to investigate whether lipopoplysaccharide (LPS) from Escherichia coli influences permeability of moPrP through the...
The formation of an abnormal form of proteins in cells can cause aggregation and neurodegenerative pathology, such as Alzheimer’s, Parkinson’s and prion diseases, which affects both humans and animals. Nowadays, the understanding of the mechanism of prion misfolding and propagation, including...
Ultraviolet-ozone treatment reduces levels of disease-associated prion protein and prion infectivityDownload
Background: Transmissible spongiform encephalopathies (TSEs) are a group of fatal neurodegenerative diseases caused by novel infectious agents referred to as prions. Prions appear to be composed primarily, if not exclusively, of a misfolded isoform of the cellular prion protein. TSE infectivity...
Zebrafish Targeted Mutagenesis to Unveil Normal Physiological Functions of, and Interactions between, Prion Protein (PrP) and Amyloid Precursor Protein (APP): Relevance to Alzheimer’s diseaseDownload
Much of the work on Prion Protein (PrPC) and Amyloid Precursor Protein (APP) biology has focused on the contributions of their misfolded forms or aggregated metabolites to prion diseases and Alzheimer’s disease, respectively. As subversion/partial loss of some normal functions are also likely...